Homodimerization of the c-Abl protein tyrosine kinase / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 698-702, 2005.
Article
in English
| WPRIM
| ID: wpr-237088
ABSTRACT
The c-Abl nonreceptor tyrosine kinase is activated in the cellular responses to genotoxic, oxidative and other forms of stress. Using tagged forms of c-Abl, the present studies demonstrate that c-Abl forms homodimers in cells. The results show that the c-Abl N-terminal regions interact with the corresponding C-terminal regions of both partners in the dimmer. Specifically, the c-Abl SH3 domain binds to a proline-rich motif at amino acids 958-982 in the c-Abl C-terminal region. Deletion of the proline-rich motif disrupts dimmer formation. These findings provide the first evidence that c-Abl forms homodimers and indicate that homodimerization can contribute to the regulation of c-Abl activity.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Proto-Oncogene Proteins c-abl
/
Src Homology Domains
/
Protein Multimerization
/
Genetics
/
Metabolism
Limits:
Humans
Language:
English
Journal:
Chinese Journal of Biotechnology
Year:
2005
Type:
Article
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